ID W9X0C3_9EURO Unreviewed; 970 AA.
AC W9X0C3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=A1O5_06409 {ECO:0000313|EMBL:EXJ70341.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ70341.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ70341.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ70341.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SH3RF family.
CC {ECO:0000256|ARBA:ARBA00008649}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXJ70341.1}.
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DR EMBL; AMGX01000009; EXJ70341.1; -; Genomic_DNA.
DR RefSeq; XP_007745193.1; XM_007747003.1.
DR AlphaFoldDB; W9X0C3; -.
DR STRING; 1182543.W9X0C3; -.
DR GeneID; 19191120; -.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_005224_1_0_1; -.
DR OrthoDB; 1462937at2759; -.
DR Proteomes; UP000019471; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR16079:SF4; E3 UBIQUITIN-PROTEIN LIGASE CHFR; 1.
DR PANTHER; PTHR16079; UBIQUITIN LIGASE PROTEIN CHFR; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019471};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 21..75
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 99..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 107392 MW; 2769F42A79C5ECC0 CRC64;
MAAITETPTT GLLNLEKELV CFICTEVLYQ PLTLLDCLHT FCGSCLKEWF SHQYRKAIHS
RTPSSTNPYT CPTCRAPVKT ARPYAKINTL LEMFLIANPD KDRTPEEKAE MSQAYKPGDE
ILPKVENHRR RERRRREEEE SAPGDSRNGE GGQRERSRRD QHLDPASADT RRGTSGSSRS
RERRETAERQ RDADRRQRHE QQPASDATSS RPRTAASSNS ADLSSLSPPP SSPRHPEAVE
ARQRGARTVA HQASLISIVS ASESGTGTGD SLDEGRLMQE ILAEGLLDGI NIDELTEQEQ
DALSETIAER IRQLHPERLR RPGSDDSRHD SHGATTRPPA SQIEEPARRS RQSSRNNNRE
RTQPSPRSSH NVVIGGNETR PPTASSQSAA EQLLTPPHTS VQRRRASDES RRSENSGLRT
ERTPHPAARS ATDLSNRPSS NASSAARIQQ LQQLPQAHRS NTEPRTSPRA SEVWQAAGGR
NISSPPQVAS PAQQSPRPDF AQPLMSSIAT GPVPTSIPTL DPAARAPEPS ELSAGNAPNR
SEEPYIVCSR CSRPNIQYEV HKHCAPCNVD LCLRCYRTGR GCNHWFGFYR SAMPKFNASH
PPNRNNQSVG LPHLLVGRQY QRPSRQHSTT PNASSRLREG NFCDRCGSLA NDYFWSCDYC
NEGEWGFCND CVNTNHCCDH PLLPVAYKSS DLNAASSRIG GGSAAVTLSP YSAGGRDVSP
AQSAASSVTS AAGPYPGVRP DFVPLDVKTN CDICSRSISP QETRYHCPTH PTPSPENSGL
KGDYDICSTC YRRFVETGQI KHEDGPDGWR LCPDGHRMIA VAFERDDEGN ERRIITRDIV
GGVQMADADV AAWKLAMKNL HRVDRATLSA VRGDWSWRED EAGTRRKTRA RAATLPRSGV
QLPPDGGWGK AYVARWSYYP PEHDNKAKDE LMFPKHATVR EVEEINDEWW FGVYAGDAGV
FPAIFLKSRA
//
